CPSM_HUMAN
ID CPSM_HUMAN Reviewed; 1500 AA.
AC P31327; B7Z818; J3KQL0; O43774; Q53TL5; Q59HF8; Q7Z5I5;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 241.
DE RecName: Full=Carbamoyl-phosphate synthase [ammonia], mitochondrial;
DE EC=6.3.4.16 {ECO:0000269|PubMed:23649895, ECO:0000269|PubMed:24813853};
DE AltName: Full=Carbamoyl-phosphate synthetase I;
DE Short=CPSase I;
DE Flags: Precursor;
GN Name=CPS1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS SER-1266; LEU-1283 AND
RP ASN-1406.
RC TISSUE=Liver;
RX PubMed=1840546; DOI=10.1016/0378-1119(91)90336-a;
RA Haraguchi Y., Uchino T., Takiguchi M., Endo F., Mori M., Matsuda I.;
RT "Cloning and sequence of a cDNA encoding human carbamyl phosphate
RT synthetase I: molecular analysis of hyperammonemia.";
RL Gene 107:335-340(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT CPS1D MET-544, AND VARIANT
RP ALA-344.
RC TISSUE=Liver;
RX PubMed=9711878;
RX DOI=10.1002/(sici)1098-1004(1998)12:3<206::aid-humu8>3.0.co;2-e;
RA Finckh U., Kohlschuetter A., Schaefer H., Sperhake K., Colombo J.-P.,
RA Gal A.;
RT "Prenatal diagnosis of carbamoyl phosphate synthetase I deficiency by
RT identification of a missense mutation in CPS1.";
RL Hum. Mutat. 12:206-211(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS ALA-344; SER-1376 AND
RP ASN-1406.
RX PubMed=12853138; DOI=10.1016/s0378-1119(03)00528-6;
RA Summar M.L., Hall L.D., Eeds A.M., Hutcheson H.B., Kuo A.N., Willis A.S.,
RA Rubio V., Arvin M.K., Schofield J.P., Dawson E.P.;
RT "Characterization of genomic structure and polymorphisms in the human
RT carbamyl phosphate synthetase I gene.";
RL Gene 311:51-57(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Testis;
RA Huo R., Zhu H., Huang X.Y., Xu Z.Y., Lu L., Xu M., Yin L.L., Li J.M.,
RA Zhou Z.M., Sha J.H.;
RT "Cloning of an isoform of CPS1 gene related to spermatogenesis.";
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), VARIANTS CPS1D GLY-457 AND
RP ARG-810, AND VARIANT ASN-1406.
RX PubMed=12955727; DOI=10.1002/humu.9184;
RA Funghini S., Donati M.A., Pasquini E., Zammarchi E., Morrone A.;
RT "Structural organization of the human carbamyl phosphate synthetase I gene
RT (CPS1) and identification of two novel genetic lesions.";
RL Hum. Mutat. 22:340-341(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), VARIANT CPS1D SER-843, AND
RP VARIANT GLU-875.
RX PubMed=12655559; DOI=10.1002/humu.9118;
RA Haeberle J., Schmidt E., Pauli S., Rapp B., Christensen E., Wermuth B.,
RA Koch H.G.;
RT "Gene structure of human carbamylphosphate synthetase 1 and novel mutations
RT in patients with neonatal onset.";
RL Hum. Mutat. 21:444-444(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT ALA-344.
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RT "Homo sapiens protein coding cDNA.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [12]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 795-1500.
RC TISSUE=Small intestine;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [13]
RP ALLOSTERIC ACTIVATOR NAG BINDING SITE.
RX PubMed=19754428; DOI=10.1042/bj20090888;
RA Pekkala S., Martinez A.I., Barcelona B., Gallego J., Bendala E.,
RA Yefimenko I., Rubio V., Cervera J.;
RT "Structural insight on the control of urea synthesis: identification of the
RT binding site for N-acetyl-L-glutamate, the essential allosteric activator
RT of mitochondrial carbamoyl phosphate synthetase.";
RL Biochem. J. 424:211-220(2009).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [15]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=22002106; DOI=10.1074/mcp.m111.013680;
RA Ahmad Y., Boisvert F.M., Lundberg E., Uhlen M., Lamond A.I.;
RT "Systematic analysis of protein pools, isoforms, and modifications
RT affecting turnover and subcellular localization.";
RL Mol. Cell. Proteomics 11:M111.013680.01-M111.013680.15(2012).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1036 AND SER-1079, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [17]
RP GLUTARYLATION AT LYS-55; LYS-171; LYS-176; LYS-207; LYS-210; LYS-214;
RP LYS-219; LYS-228; LYS-237; LYS-280; LYS-307; LYS-310; LYS-402; LYS-412;
RP LYS-453; LYS-458; LYS-527; LYS-532; LYS-553; LYS-728; LYS-757; LYS-772;
RP LYS-793; LYS-811; LYS-841; LYS-856; LYS-869; LYS-875; LYS-889; LYS-892;
RP LYS-905; LYS-908; LYS-915; LYS-919; LYS-1074; LYS-1150; LYS-1168; LYS-1183;
RP LYS-1224; LYS-1356; LYS-1360; LYS-1479 AND LYS-1486.
RX PubMed=24703693; DOI=10.1016/j.cmet.2014.03.014;
RA Tan M., Peng C., Anderson K.A., Chhoy P., Xie Z., Dai L., Park J., Chen Y.,
RA Huang H., Zhang Y., Ro J., Wagner G.R., Green M.F., Madsen A.S.,
RA Schmiesing J., Peterson B.S., Xu G., Ilkayeva O.R., Muehlbauer M.J.,
RA Braulke T., Muehlhausen C., Backos D.S., Olsen C.A., McGuire P.J.,
RA Pletcher S.D., Lombard D.B., Hirschey M.D., Zhao Y.;
RT "Lysine glutarylation is a protein posttranslational modification regulated
RT by SIRT5.";
RL Cell Metab. 19:605-617(2014).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-148; SER-569; SER-835;
RP SER-1079; SER-1203; SER-1419 AND SER-1431, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) OF 1343-1478.
RG RIKEN structural genomics initiative (RSGI);
RT "Crystal structure of MGS domain of carbamoyl-phosphate synthetase from
RT Homo sapiens.";
RL Submitted (FEB-2009) to the PDB data bank.
RN [20]
RP VARIANT CPS1D ARG-1054.
RX PubMed=11388595; DOI=10.1007/s004310100725;
RA Rapp B., Haberle J., Linnebank M., Wermuth B., Marquardt T., Harms E.,
RA Koch H.G.;
RT "Genetic analysis of carbamoylphosphate synthetase I and ornithine
RT transcarbamylase deficiency using fibroblasts.";
RL Eur. J. Pediatr. 160:283-287(2001).
RN [21]
RP VARIANT CPS1D ARG-337.
RX PubMed=11474210; DOI=10.1159/000053360;
RA Aoshima T., Kajita M., Sekido Y., Kikuchi S., Yasuda I., Saheki T.,
RA Watanabe K., Shimokata K., Niwa T.;
RT "Novel mutations (H337R and 238-362del) in the CPS1 gene cause carbamoyl
RT phosphate synthetase I deficiency.";
RL Hum. Hered. 52:99-101(2001).
RN [22]
RP VARIANT ASN-1406, AND INVOLVEMENT IN PHN.
RX PubMed=11407344; DOI=10.1056/nejm200106143442404;
RA Pearson D.L., Dawling S., Walsh W.F., Haines J.L., Christman B.W.,
RA Bazyk A., Scott N., Summar M.L.;
RT "Neonatal pulmonary hypertension -- urea-cycle intermediates, nitric oxide
RT production, and carbamoyl-phosphate synthetase function.";
RL N. Engl. J. Med. 344:1832-1838(2001).
RN [23]
RP VARIANTS CPS1D HIS-850 AND PRO-918.
RX PubMed=15617192; DOI=10.1023/b:boli.0000045842.59768.ea;
RA Wakutani Y., Nakayasu H., Takeshima T., Adachi M., Kawataki M., Kihira K.,
RA Sawada H., Bonno M., Yamamoto H., Nakashima K.;
RT "Mutational analysis of carbamoylphosphate synthetase I deficiency in three
RT Japanese patients.";
RL J. Inherit. Metab. Dis. 27:787-788(2004).
RN [24]
RP VARIANT CPS1D SER-843, AND VARIANT GLU-875.
RX PubMed=15164414; DOI=10.1002/pd.884;
RA Haeberle J., Koch H.G.;
RT "Genetic approach to prenatal diagnosis in urea cycle defects.";
RL Prenat. Diagn. 24:378-383(2004).
RN [25]
RP VARIANTS CPS1D GLU-301; CYS-389; ARG-390; THR-589; SER-640; LYS-716;
RP LEU-805; VAL-911; PRO-958; SER-982; PHE-998; LEU-1089; PRO-1203; ASN-1205;
RP PRO-1331; THR-1378; LEU-1411 AND ALA-1443.
RX PubMed=16737834; DOI=10.1016/j.ymgme.2006.04.006;
RA Eeds A.M., Hall L.D., Yadav M., Willis A., Summar S., Putnam A., Barr F.,
RA Summar M.L.;
RT "The frequent observation of evidence for nonsense-mediated decay in RNA
RT from patients with carbamyl phosphate synthetase I deficiency.";
RL Mol. Genet. Metab. 89:80-86(2006).
RN [26]
RP VARIANTS CPS1D GLU-79; ASN-212; ASN-280; PRO-438; HIS-587; ARG-593;
RP LYS-651; ILE-674; HIS-780; CYS-850; ASP-982; ARG-1103; GLY-1141; PRO-1195;
RP VAL-1215 AND LYS-1241.
RX PubMed=17310273; DOI=10.1007/s10038-007-0122-9;
RA Kurokawa K., Yorifuji T., Kawai M., Momoi T., Nagasaka H., Takayanagi M.,
RA Kobayashi K., Yoshino M., Kosho T., Adachi M., Otsuka H., Yamamoto S.,
RA Murata T., Suenaga A., Ishii T., Terada K., Shimura N., Kiwaki K.,
RA Shintaku H., Yamakawa M., Nakabayashi H., Wakutani Y., Nakahata T.;
RT "Molecular and clinical analyses of Japanese patients with
RT carbamoylphosphate synthetase 1 (CPS1) deficiency.";
RL J. Hum. Genet. 52:349-354(2007).
RN [27]
RP VARIANTS CPS1D PHE-123; ARG-337; ASN-471; PRO-678; LEU-774; LEU-1411;
RP GLN-1453; TRP-1453 AND HIS-1491, VARIANT SER-1376, CHARACTERIZATION OF
RP VARIANTS CPS1D PHE-123; ARG-337; ASN-471; PRO-678; LEU-774; LEU-1411;
RP GLN-1453; TRP-1453 AND HIS-1491, AND CHARACTERIZATION OF VARIANT SER-1376.
RX PubMed=20578160; DOI=10.1002/humu.21272;
RA Pekkala S., Martinez A.I., Barcelona B., Yefimenko I., Finckh U., Rubio V.,
RA Cervera J.;
RT "Understanding carbamoyl-phosphate synthetase I (CPS1) deficiency by using
RT expression studies and structure-based analysis.";
RL Hum. Mutat. 31:801-808(2010).
RN [28]
RP VARIANT ASN-1406.
RX PubMed=20520828; DOI=10.1371/journal.pone.0010792;
RA Moonen R.M., Reyes I., Cavallaro G., Gonzalez-Luis G., Bakker J.A.,
RA Villamor E.;
RT "The T1405N carbamoyl phosphate synthetase polymorphism does not affect
RT plasma arginine concentrations in preterm infants.";
RL PLoS ONE 5:E10792-E10792(2010).
RN [29]
RP VARIANTS CPS1D VAL-43; ASP-58; PHE-65; GLY-71; SER-87; ASP-89; GLY-165;
RP VAL-224; CYS-233; PRO-243; GLU-258; GLU-263; VAL-304; GLU-317; HIS-358;
RP LEU-382; ARG-401; ARG-431; VAL-432; THR-438; GLU-450; PRO-498; GLU-531;
RP GLY-531; MET-544; CYS-587; HIS-587; LEU-587; LEU-597; MET-622; ASP-628;
RP ARG-632; PRO-638; TYR-648; VAL-654; LYS-674; SER-698; LYS-718; GLN-721;
RP PRO-724; THR-726; VAL-767; HIS-780; ILE-792; SER-803; GLY-803; CYS-803;
RP SER-805; TRP-814; ARG-816; HIS-850; GLU-911; LEU-913; HIS-914; GLY-914;
RP THR-932; THR-949; CYS-959; CYS-962; GLU-978; VAL-982; HIS-984; THR-986;
RP CYS-987; SER-992; SER-1016; LEU-1017; ILE-1022; GLY-1034; ARG-1045;
RP ARG-1059; GLU-1065; CYS-1089; GLU-1155; VAL-1155; LEU-1203; GLN-1228;
RP ASP-1255; GLN-1262; PRO-1262; HIS-1274; ARG-1327; GLU-1333; LEU-1371;
RP MET-1391; VAL-1398; LEU-1439; TRP-1453 AND ARG-1462.
RX PubMed=21120950; DOI=10.1002/humu.21406;
RA Haberle J., Shchelochkov O.A., Wang J., Katsonis P., Hall L., Reiss S.,
RA Eeds A., Willis A., Yadav M., Summar S., Lichtarge O., Rubio V., Wong L.J.,
RA Summar M.;
RT "Molecular defects in human carbamoyl phosphate synthetase I: mutational
RT spectrum, diagnostic and protein structure considerations.";
RL Hum. Mutat. 32:579-589(2011).
RN [30]
RP VARIANTS VAL-530 AND ASN-1406.
RX PubMed=21767969; DOI=10.1016/j.ymgme.2011.06.022;
RG NISC Comparative Sequencing Program;
RA Solomon B.D., Pineda-Alvarez D.E., Hadley D.W., Teer J.K., Cherukuri P.F.,
RA Hansen N.F., Cruz P., Young A.C., Blakesley R.W., Lanpher B.,
RA Mayfield Gibson S., Sincan M., Chandrasekharappa S.C., Mullikin J.C.;
RT "Personalized genomic medicine: lessons from the exome.";
RL Mol. Genet. Metab. 104:189-191(2011).
RN [31]
RP VARIANTS CPS1D SER-341; ARG-661; ASP-964 AND ARG-1167.
RX PubMed=22173106; DOI=10.1016/j.gene.2011.11.052;
RA Funghini S., Thusberg J., Spada M., Gasperini S., Parini R., Ventura L.,
RA Meli C., De Cosmo L., Sibilio M., Mooney S.D., Guerrini R., Donati M.A.,
RA Morrone A.;
RT "Carbamoyl phosphate synthetase 1 deficiency in Italy: clinical and genetic
RT findings in a heterogeneous cohort.";
RL Gene 493:228-234(2012).
RN [32]
RP VARIANTS CPS1D ASP-355; CYS-389; ARG-390; PRO-438; MET-544; THR-1378;
RP SER-1381 AND ALA-1443, VARIANTS ALA-344 AND SER-1376, CHARACTERIZATION OF
RP VARIANTS CPS1D ASP-355; CYS-389; ARG-390; PRO-438; MET-544; THR-1378;
RP SER-1381 AND ALA-1443, CHARACTERIZATION OF VARIANTS ALA-344 AND SER-1376,
RP SUBUNIT, PROTEOLYTIC CLEAVAGE, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP REGULATION, AND CATALYTIC ACTIVITY.
RX PubMed=23649895; DOI=10.1002/humu.22349;
RA Diez-Fernandez C., Martinez A.I., Pekkala S., Barcelona B.,
RA Perez-Arellano I., Guadalajara A.M., Summar M., Cervera J., Rubio V.;
RT "Molecular characterization of carbamoyl-phosphate synthetase (CPS1)
RT deficiency using human recombinant CPS1 as a key tool.";
RL Hum. Mutat. 34:1149-1159(2013).
RN [33]
RP VARIANT ASN-1406.
RX PubMed=24237036; DOI=10.1021/pr400544j;
RA Song C., Wang F., Cheng K., Wei X., Bian Y., Wang K., Tan Y., Wang H.,
RA Ye M., Zou H.;
RT "Large-scale quantification of single amino-acid variations by a variation-
RT associated database search strategy.";
RL J. Proteome Res. 13:241-248(2014).
RN [34]
RP VARIANTS CPS1D ARG-401; ARG-632; SER-843; CYS-850; HIS-850; PRO-871;
RP VAL-911; GLU-911; LEU-913; HIS-914; GLY-914; PRO-918; THR-932; ASN-937;
RP THR-949; PRO-958; CYS-959; CYS-962; ASP-964; ASP-1194 AND ARG-1462, VARIANT
RP GLU-875, CHARACTERIZATION OF VARIANTS CPS1D SER-843; CYS-850; HIS-850;
RP PRO-871; VAL-911; GLU-911; LEU-913; HIS-914; GLY-914; PRO-918; THR-932;
RP ASN-937; THR-949; PRO-958; CYS-959; CYS-962 AND ASP-964, CATALYTIC
RP ACTIVITY, AND CHARACTERIZATION OF VARIANT GLU-875.
RX PubMed=24813853; DOI=10.1016/j.ymgme.2014.04.003;
RA Diez-Fernandez C., Hu L., Cervera J., Haeberle J., Rubio V.;
RT "Understanding carbamoyl phosphate synthetase (CPS1) deficiency by using
RT the recombinantly purified human enzyme: effects of CPS1 mutations that
RT concentrate in a central domain of unknown function.";
RL Mol. Genet. Metab. 112:123-132(2014).
RN [35]
RP VARIANTS CPS1D TYR-123; TRP-174; GLY-803; HIS-850; PHE-1254 AND
RP 1363-LEU--ILE-1366 DEL.
RX PubMed=26440671; DOI=10.1007/s00431-015-2644-z;
RA Ali E.Z., Khalid M.K., Yunus Z.M., Yakob Y., Chin C.B., Latif K.A.,
RA Hock N.L.;
RT "Carbamoylphosphate synthetase 1 (CPS1) deficiency: clinical, biochemical,
RT and molecular characterization in Malaysian patients.";
RL Eur. J. Pediatr. 175:339-346(2016).
RN [36]
RP VARIANT GLU-875.
RX PubMed=27535533; DOI=10.1038/nature19057;
RG Exome Aggregation Consortium;
RA Lek M., Karczewski K.J., Minikel E.V., Samocha K.E., Banks E., Fennell T.,
RA O'Donnell-Luria A.H., Ware J.S., Hill A.J., Cummings B.B., Tukiainen T.,
RA Birnbaum D.P., Kosmicki J.A., Duncan L.E., Estrada K., Zhao F., Zou J.,
RA Pierce-Hoffman E., Berghout J., Cooper D.N., Deflaux N., DePristo M.,
RA Do R., Flannick J., Fromer M., Gauthier L., Goldstein J., Gupta N.,
RA Howrigan D., Kiezun A., Kurki M.I., Moonshine A.L., Natarajan P.,
RA Orozco L., Peloso G.M., Poplin R., Rivas M.A., Ruano-Rubio V., Rose S.A.,
RA Ruderfer D.M., Shakir K., Stenson P.D., Stevens C., Thomas B.P., Tiao G.,
RA Tusie-Luna M.T., Weisburd B., Won H.H., Yu D., Altshuler D.M.,
RA Ardissino D., Boehnke M., Danesh J., Donnelly S., Elosua R., Florez J.C.,
RA Gabriel S.B., Getz G., Glatt S.J., Hultman C.M., Kathiresan S., Laakso M.,
RA McCarroll S., McCarthy M.I., McGovern D., McPherson R., Neale B.M.,
RA Palotie A., Purcell S.M., Saleheen D., Scharf J.M., Sklar P.,
RA Sullivan P.F., Tuomilehto J., Tsuang M.T., Watkins H.C., Wilson J.G.,
RA Daly M.J., MacArthur D.G.;
RT "Analysis of protein-coding genetic variation in 60,706 humans.";
RL Nature 536:285-291(2016).
CC -!- FUNCTION: Involved in the urea cycle of ureotelic animals where the
CC enzyme plays an important role in removing excess ammonia from the
CC cell.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 ATP + hydrogencarbonate + NH4(+) = 2 ADP + carbamoyl
CC phosphate + 2 H(+) + phosphate; Xref=Rhea:RHEA:18029,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228,
CC ChEBI:CHEBI:456216; EC=6.3.4.16;
CC Evidence={ECO:0000269|PubMed:23649895, ECO:0000269|PubMed:24813853};
CC -!- ACTIVITY REGULATION: Requires N-acetyl-L-glutamate (NAG) as an
CC allosteric activator. Activated by glycerol in the absence of NAG,
CC whereas in the presence of NAG it is inhibited by increasing
CC concentrations of glycerol. {ECO:0000269|PubMed:19754428,
CC ECO:0000269|PubMed:23649895}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.47 mM for ATP {ECO:0000269|PubMed:23649895};
CC KM=4.0 mM for HCO(3)(-) {ECO:0000269|PubMed:23649895};
CC KM=1.00 mM for NH(4)(+) {ECO:0000269|PubMed:23649895};
CC Vmax=1.22 umol/min/mg enzyme for ATP {ECO:0000269|PubMed:23649895};
CC Vmax=1.23 umol/min/mg enzyme for HCO(3)(-)
CC {ECO:0000269|PubMed:23649895};
CC Vmax=1.19 umol/min/mg enzyme for NH(4)(+)
CC {ECO:0000269|PubMed:23649895};
CC -!- SUBUNIT: Can form homooligomers (monomers as predominant form and
CC dimers). {ECO:0000269|PubMed:23649895}.
CC -!- INTERACTION:
CC P31327; P10398: ARAF; NbExp=3; IntAct=EBI-536811, EBI-365961;
CC P31327; P04049: RAF1; NbExp=4; IntAct=EBI-536811, EBI-365996;
CC P31327; P63104: YWHAZ; NbExp=2; IntAct=EBI-536811, EBI-347088;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:22002106}.
CC Nucleus, nucleolus {ECO:0000269|PubMed:22002106}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P31327-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P31327-2; Sequence=VSP_009332;
CC Name=3;
CC IsoId=P31327-3; Sequence=VSP_046685;
CC -!- TISSUE SPECIFICITY: Primarily in the liver and small intestine.
CC -!- DOMAIN: The type-1 glutamine amidotransferase domain is defective.
CC -!- PTM: Undergoes proteolytic cleavage in the C-terminal region
CC corresponding to the loss of approximately 12 AA residues from the C-
CC terminus. {ECO:0000269|PubMed:23649895}.
CC -!- PTM: Succinylated at Lys-287 and Lys-1291. Desuccinylated at Lys-1291
CC by SIRT5, leading to activation (By similarity).
CC {ECO:0000250|UniProtKB:Q8C196}.
CC -!- PTM: Glutarylated. Glutarylation levels increase during fasting.
CC Deglutarylated by SIRT5 at Lys-55, Lys-219, Lys-412, Lys-889, Lys-892,
CC Lys-915, Lys-1360 and Lys-1486, leading to activation.
CC {ECO:0000269|PubMed:24703693}.
CC -!- DISEASE: Carbamoyl phosphate synthetase 1 deficiency (CPS1D)
CC [MIM:237300]: An autosomal recessive disorder of the urea cycle causing
CC hyperammonemia. It can present as a devastating metabolic disease
CC dominated by severe hyperammonemia in neonates or as a more insidious
CC late-onset condition, generally manifesting as life-threatening
CC hyperammonemic crises under catabolic situations. Clinical features
CC include protein intolerance, intermittent ataxia, seizures, lethargy,
CC developmental delay and intellectual disability.
CC {ECO:0000269|PubMed:11388595, ECO:0000269|PubMed:11474210,
CC ECO:0000269|PubMed:12655559, ECO:0000269|PubMed:12955727,
CC ECO:0000269|PubMed:15164414, ECO:0000269|PubMed:15617192,
CC ECO:0000269|PubMed:16737834, ECO:0000269|PubMed:17310273,
CC ECO:0000269|PubMed:20578160, ECO:0000269|PubMed:21120950,
CC ECO:0000269|PubMed:22173106, ECO:0000269|PubMed:23649895,
CC ECO:0000269|PubMed:24813853, ECO:0000269|PubMed:26440671,
CC ECO:0000269|PubMed:9711878}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Pulmonary hypertension, neonatal (PHN) [MIM:615371]: A disease
CC characterized by elevated pulmonary artery pressure. Pulmonary
CC hypertension in the neonate is associated with multiple underlying
CC problems such as respiratory distress syndrome, meconium aspiration
CC syndrome, congenital diaphragmatic hernia, bronchopulmonary dysplasia,
CC sepsis, or congenital heart disease. {ECO:0000269|PubMed:11407344}.
CC Note=Disease susceptibility is associated with variants affecting the
CC gene represented in this entry. CPS1 variants influence the
CC availability of precursors for nitric oxide (NO) synthesis and play a
CC role in clinical situations where endogenous NO production is
CC critically important, such as neonatal pulmonary hypertension,
CC increased pulmonary artery pressure following surgical repair of
CC congenital heart defects or hepatovenocclusive disease following bone
CC marrow transplantation. Infants with neonatal pulmonary hypertension
CC homozygous for Thr-1406 have lower L-arginine concentrations than
CC neonates homozygous for Asn-1406 (PubMed:11407344).
CC {ECO:0000269|PubMed:11407344}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD92037.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=LOVD-Leiden Open Variation Database; Note=Carbamoyl-
CC Phosphate Synthetase 1 (CPS1);
CC URL="https://databases.lovd.nl/shared/genes/CPS1";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D90282; BAA14328.1; -; mRNA.
DR EMBL; Y15793; CAA75785.1; -; mRNA.
DR EMBL; AF154830; AAD38072.1; -; mRNA.
DR EMBL; AY317138; AAP84318.1; -; mRNA.
DR EMBL; AY167007; AAO31763.1; -; Genomic_DNA.
DR EMBL; AY166970; AAO31763.1; JOINED; Genomic_DNA.
DR EMBL; AY166971; AAO31763.1; JOINED; Genomic_DNA.
DR EMBL; AY166972; AAO31763.1; JOINED; Genomic_DNA.
DR EMBL; AY166973; AAO31763.1; JOINED; Genomic_DNA.
DR EMBL; AY166974; AAO31763.1; JOINED; Genomic_DNA.
DR EMBL; AY166975; AAO31763.1; JOINED; Genomic_DNA.
DR EMBL; AY166976; AAO31763.1; JOINED; Genomic_DNA.
DR EMBL; AY166977; AAO31763.1; JOINED; Genomic_DNA.
DR EMBL; AY166978; AAO31763.1; JOINED; Genomic_DNA.
DR EMBL; AY166979; AAO31763.1; JOINED; Genomic_DNA.
DR EMBL; AY166980; AAO31763.1; JOINED; Genomic_DNA.
DR EMBL; AY166981; AAO31763.1; JOINED; Genomic_DNA.
DR EMBL; AY166982; AAO31763.1; JOINED; Genomic_DNA.
DR EMBL; AY166983; AAO31763.1; JOINED; Genomic_DNA.
DR EMBL; AY166984; AAO31763.1; JOINED; Genomic_DNA.
DR EMBL; AY166985; AAO31763.1; JOINED; Genomic_DNA.
DR EMBL; AY166986; AAO31763.1; JOINED; Genomic_DNA.
DR EMBL; AY166987; AAO31763.1; JOINED; Genomic_DNA.
DR EMBL; AY166988; AAO31763.1; JOINED; Genomic_DNA.
DR EMBL; AY166989; AAO31763.1; JOINED; Genomic_DNA.
DR EMBL; AY166990; AAO31763.1; JOINED; Genomic_DNA.
DR EMBL; AY166991; AAO31763.1; JOINED; Genomic_DNA.
DR EMBL; AY166992; AAO31763.1; JOINED; Genomic_DNA.
DR EMBL; AY166993; AAO31763.1; JOINED; Genomic_DNA.
DR EMBL; AY166994; AAO31763.1; JOINED; Genomic_DNA.
DR EMBL; AY166995; AAO31763.1; JOINED; Genomic_DNA.
DR EMBL; AY166996; AAO31763.1; JOINED; Genomic_DNA.
DR EMBL; AY166997; AAO31763.1; JOINED; Genomic_DNA.
DR EMBL; AY166998; AAO31763.1; JOINED; Genomic_DNA.
DR EMBL; AY166999; AAO31763.1; JOINED; Genomic_DNA.
DR EMBL; AY167000; AAO31763.1; JOINED; Genomic_DNA.
DR EMBL; AY167001; AAO31763.1; JOINED; Genomic_DNA.
DR EMBL; AY167002; AAO31763.1; JOINED; Genomic_DNA.
DR EMBL; AY167003; AAO31763.1; JOINED; Genomic_DNA.
DR EMBL; AY167004; AAO31763.1; JOINED; Genomic_DNA.
DR EMBL; AY167005; AAO31763.1; JOINED; Genomic_DNA.
DR EMBL; AY167006; AAO31763.1; JOINED; Genomic_DNA.
DR EMBL; AF536523; AAN77181.1; -; Genomic_DNA.
DR EMBL; AK302778; BAH13804.1; -; mRNA.
DR EMBL; AC007970; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC008172; AAY14960.1; -; Genomic_DNA.
DR EMBL; CH471063; EAW70492.1; -; Genomic_DNA.
DR EMBL; BC140943; AAI40944.1; -; mRNA.
DR EMBL; AB208800; BAD92037.1; ALT_INIT; mRNA.
DR EMBL; BX640601; CAE45707.1; -; mRNA.
DR CCDS; CCDS2393.1; -. [P31327-1]
DR CCDS; CCDS46505.1; -. [P31327-1]
DR PIR; JQ1348; JQ1348.
DR RefSeq; NP_001116105.1; NM_001122633.2. [P31327-1]
DR RefSeq; NP_001116106.1; NM_001122634.3.
DR RefSeq; NP_001866.2; NM_001875.4. [P31327-1]
DR RefSeq; XP_011508943.1; XM_011510641.2.
DR RefSeq; XP_011508944.1; XM_011510642.2.
DR RefSeq; XP_011508945.1; XM_011510643.2.
DR RefSeq; XP_011508946.1; XM_011510644.2.
DR PDB; 2YVQ; X-ray; 1.98 A; A=1343-1478.
DR PDB; 4UTR; X-ray; 2.90 A; C=524-531.
DR PDB; 4UTV; X-ray; 2.40 A; C=524-531.
DR PDB; 4UTX; X-ray; 3.10 A; C=524-531.
DR PDB; 4UTZ; X-ray; 3.30 A; D=524-531.
DR PDB; 4UU7; X-ray; 3.00 A; D=524-531.
DR PDB; 4UU8; X-ray; 2.90 A; D=524-531.
DR PDB; 4UUA; X-ray; 2.80 A; D=524-531.
DR PDB; 4UUB; X-ray; 2.90 A; D=524-531.
DR PDB; 5DOT; X-ray; 2.40 A; A/B=40-1500.
DR PDB; 5DOU; X-ray; 2.60 A; A/B/C/D=40-1500.
DR PDB; 5OJO; X-ray; 3.10 A; C=524-531.
DR PDB; 6UEL; X-ray; 1.90 A; A/B=1-1500.
DR PDB; 6W2J; X-ray; 2.62 A; A/B=1-1500.
DR PDBsum; 2YVQ; -.
DR PDBsum; 4UTR; -.
DR PDBsum; 4UTV; -.
DR PDBsum; 4UTX; -.
DR PDBsum; 4UTZ; -.
DR PDBsum; 4UU7; -.
DR PDBsum; 4UU8; -.
DR PDBsum; 4UUA; -.
DR PDBsum; 4UUB; -.
DR PDBsum; 5DOT; -.
DR PDBsum; 5DOU; -.
DR PDBsum; 5OJO; -.
DR PDBsum; 6UEL; -.
DR PDBsum; 6W2J; -.
DR AlphaFoldDB; P31327; -.
DR SMR; P31327; -.
DR BioGRID; 107764; 181.
DR IntAct; P31327; 49.
DR MINT; P31327; -.
DR STRING; 9606.ENSP00000402608; -.
DR BindingDB; P31327; -.
DR ChEMBL; CHEMBL2362990; -.
DR DrugBank; DB11118; Ammonia.
DR DrugBank; DB06775; Carglumic acid.
DR DrugCentral; P31327; -.
DR MEROPS; C26.951; -.
DR GlyGen; P31327; 4 sites, 1 O-linked glycan (1 site).
DR iPTMnet; P31327; -.
DR MetOSite; P31327; -.
DR PhosphoSitePlus; P31327; -.
DR SwissPalm; P31327; -.
DR BioMuta; CPS1; -.
DR DMDM; 4033707; -.
DR EPD; P31327; -.
DR jPOST; P31327; -.
DR MassIVE; P31327; -.
DR MaxQB; P31327; -.
DR PaxDb; P31327; -.
DR PeptideAtlas; P31327; -.
DR PRIDE; P31327; -.
DR ProteomicsDB; 54782; -. [P31327-1]
DR ProteomicsDB; 54783; -. [P31327-2]
DR Antibodypedia; 20025; 475 antibodies from 33 providers.
DR DNASU; 1373; -.
DR Ensembl; ENST00000233072.10; ENSP00000233072.5; ENSG00000021826.18. [P31327-1]
DR Ensembl; ENST00000430249.7; ENSP00000402608.2; ENSG00000021826.18. [P31327-3]
DR Ensembl; ENST00000451903.3; ENSP00000406136.2; ENSG00000021826.18. [P31327-2]
DR Ensembl; ENST00000673510.1; ENSP00000500537.1; ENSG00000021826.18. [P31327-1]
DR Ensembl; ENST00000673630.1; ENSP00000501073.1; ENSG00000021826.18. [P31327-1]
DR Ensembl; ENST00000673711.1; ENSP00000501022.1; ENSG00000021826.18. [P31327-1]
DR GeneID; 1373; -.
DR KEGG; hsa:1373; -.
DR MANE-Select; ENST00000233072.10; ENSP00000233072.5; NM_001875.5; NP_001866.2.
DR UCSC; uc002vee.5; human. [P31327-1]
DR CTD; 1373; -.
DR DisGeNET; 1373; -.
DR GeneCards; CPS1; -.
DR GeneReviews; CPS1; -.
DR HGNC; HGNC:2323; CPS1.
DR HPA; ENSG00000021826; Tissue enriched (liver).
DR MalaCards; CPS1; -.
DR MIM; 237300; phenotype.
DR MIM; 608307; gene.
DR MIM; 615371; phenotype.
DR neXtProt; NX_P31327; -.
DR OpenTargets; ENSG00000021826; -.
DR Orphanet; 147; Carbamoyl-phosphate synthetase 1 deficiency.
DR PharmGKB; PA26840; -.
DR VEuPathDB; HostDB:ENSG00000021826; -.
DR eggNOG; KOG0370; Eukaryota.
DR GeneTree; ENSGT00940000157192; -.
DR HOGENOM; CLU_000513_0_1_1; -.
DR InParanoid; P31327; -.
DR OMA; IEPAGIH; -.
DR OrthoDB; 1095345at2759; -.
DR PhylomeDB; P31327; -.
DR TreeFam; TF331485; -.
DR BioCyc; MetaCyc:HS00415-MON; -.
DR BRENDA; 6.3.4.16; 2681.
DR PathwayCommons; P31327; -.
DR Reactome; R-HSA-70635; Urea cycle.
DR SABIO-RK; P31327; -.
DR SignaLink; P31327; -.
DR SIGNOR; P31327; -.
DR BioGRID-ORCS; 1373; 20 hits in 1089 CRISPR screens.
DR ChiTaRS; CPS1; human.
DR EvolutionaryTrace; P31327; -.
DR GenomeRNAi; 1373; -.
DR Pharos; P31327; Tclin.
DR PRO; PR:P31327; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P31327; protein.
DR Bgee; ENSG00000021826; Expressed in liver and 144 other tissues.
DR ExpressionAtlas; P31327; baseline and differential.
DR Genevisible; P31327; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:Ensembl.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0042645; C:mitochondrial nucleoid; IDA:BHF-UCL.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:Ensembl.
DR GO; GO:0004087; F:carbamoyl-phosphate synthase (ammonia) activity; IMP:BHF-UCL.
DR GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:InterPro.
DR GO; GO:0004175; F:endopeptidase activity; IEA:Ensembl.
DR GO; GO:0016595; F:glutamate binding; IEA:Ensembl.
DR GO; GO:0072341; F:modified amino acid binding; IDA:UniProtKB.
DR GO; GO:0005543; F:phospholipid binding; IEA:Ensembl.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro.
DR GO; GO:0055081; P:anion homeostasis; IEA:Ensembl.
DR GO; GO:0070409; P:carbamoyl phosphate biosynthetic process; IMP:UniProtKB.
DR GO; GO:0071242; P:cellular response to ammonium ion; IMP:BHF-UCL.
DR GO; GO:0071320; P:cellular response to cAMP; IEA:Ensembl.
DR GO; GO:0044344; P:cellular response to fibroblast growth factor stimulus; IEA:Ensembl.
DR GO; GO:0071377; P:cellular response to glucagon stimulus; IEA:Ensembl.
DR GO; GO:0071400; P:cellular response to oleic acid; IEA:Ensembl.
DR GO; GO:0019240; P:citrulline biosynthetic process; NAS:BHF-UCL.
DR GO; GO:0006541; P:glutamine metabolic process; IBA:GO_Central.
DR GO; GO:0070365; P:hepatocyte differentiation; IEA:Ensembl.
DR GO; GO:0050667; P:homocysteine metabolic process; IDA:UniProtKB.
DR GO; GO:0007494; P:midgut development; IEA:Ensembl.
DR GO; GO:0046209; P:nitric oxide metabolic process; IMP:BHF-UCL.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IBA:GO_Central.
DR GO; GO:0014075; P:response to amine; IEA:Ensembl.
DR GO; GO:0043200; P:response to amino acid; IEA:Ensembl.
DR GO; GO:0071548; P:response to dexamethasone; IEA:Ensembl.
DR GO; GO:0032094; P:response to food; IEA:Ensembl.
DR GO; GO:0060416; P:response to growth hormone; IEA:Ensembl.
DR GO; GO:0032496; P:response to lipopolysaccharide; IDA:UniProtKB.
DR GO; GO:0042594; P:response to starvation; IEA:Ensembl.
DR GO; GO:0009636; P:response to toxic substance; IEA:Ensembl.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0010043; P:response to zinc ion; IEA:Ensembl.
DR GO; GO:0019433; P:triglyceride catabolic process; IMP:BHF-UCL.
DR GO; GO:0000050; P:urea cycle; TAS:Reactome.
DR GO; GO:0042311; P:vasodilation; IMP:BHF-UCL.
DR CDD; cd01744; GATase1_CPSase; 1.
DR Gene3D; 1.10.1030.10; -; 1.
DR Gene3D; 3.30.1490.20; -; 1.
DR Gene3D; 3.40.50.1380; -; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 3.50.30.20; -; 1.
DR HAMAP; MF_01209; CPSase_S_chain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR006275; CarbamoylP_synth_lsu.
DR InterPro; IPR005480; CarbamoylP_synth_lsu_oligo.
DR InterPro; IPR036897; CarbamoylP_synth_lsu_oligo_sf.
DR InterPro; IPR006274; CarbamoylP_synth_ssu.
DR InterPro; IPR002474; CarbamoylP_synth_ssu_N.
DR InterPro; IPR036480; CarbP_synth_ssu_N_sf.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR005483; CbamoylP_synth_lsu_CPSase_dom.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR035686; CPSase_GATase1.
DR InterPro; IPR017926; GATASE.
DR InterPro; IPR011607; MGS-like_dom.
DR InterPro; IPR036914; MGS-like_dom_sf.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR Pfam; PF02786; CPSase_L_D2; 2.
DR Pfam; PF02787; CPSase_L_D3; 1.
DR Pfam; PF00988; CPSase_sm_chain; 1.
DR Pfam; PF00117; GATase; 1.
DR Pfam; PF02142; MGS; 1.
DR PRINTS; PR00098; CPSASE.
DR SMART; SM01096; CPSase_L_D3; 1.
DR SMART; SM01097; CPSase_sm_chain; 1.
DR SMART; SM00851; MGS; 1.
DR SUPFAM; SSF48108; SSF48108; 1.
DR SUPFAM; SSF52021; SSF52021; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
DR SUPFAM; SSF52335; SSF52335; 1.
DR SUPFAM; SSF52440; SSF52440; 2.
DR TIGRFAMs; TIGR01369; CPSaseII_lrg; 1.
DR TIGRFAMs; TIGR01368; CPSaseIIsmall; 1.
DR PROSITE; PS50975; ATP_GRASP; 2.
DR PROSITE; PS00866; CPSASE_1; 2.
DR PROSITE; PS00867; CPSASE_2; 2.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
DR PROSITE; PS51855; MGS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Allosteric enzyme; Alternative splicing;
KW ATP-binding; Disease variant; Glycoprotein; Ligase; Mitochondrion;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Transit peptide; Urea cycle.
FT TRANSIT 1..38
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 39..1500
FT /note="Carbamoyl-phosphate synthase [ammonia],
FT mitochondrial"
FT /id="PRO_0000029897"
FT DOMAIN 219..404
FT /note="Glutamine amidotransferase type-1"
FT DOMAIN 551..743
FT /note="ATP-grasp 1"
FT DOMAIN 1093..1284
FT /note="ATP-grasp 2"
FT DOMAIN 1355..1500
FT /note="MGS-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01202"
FT REGION 39..218
FT /note="Anthranilate phosphoribosyltransferase homolog"
FT BINDING 1391
FT /ligand="N-acetyl-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:44337"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000305"
FT BINDING 1394
FT /ligand="N-acetyl-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:44337"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000305"
FT BINDING 1410
FT /ligand="N-acetyl-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:44337"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000305"
FT BINDING 1437
FT /ligand="N-acetyl-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:44337"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000305"
FT BINDING 1440
FT /ligand="N-acetyl-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:44337"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000305"
FT BINDING 1449
FT /ligand="N-acetyl-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:44337"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000305"
FT MOD_RES 55
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8C196"
FT MOD_RES 55
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000269|PubMed:24703693"
FT MOD_RES 55
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8C196"
FT MOD_RES 57
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8C196"
FT MOD_RES 57
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8C196"
FT MOD_RES 119
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8C196"
FT MOD_RES 119
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8C196"
FT MOD_RES 148
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 157
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8C196"
FT MOD_RES 157
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8C196"
FT MOD_RES 171
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8C196"
FT MOD_RES 171
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000269|PubMed:24703693"
FT MOD_RES 176
FT /note="N6-glutaryllysine"
FT /evidence="ECO:0000269|PubMed:24703693"
FT MOD_RES 182
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8C196"
FT MOD_RES 197
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8C196"
FT MOD_RES 207
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8C196"
FT MOD_RES 207
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000269|PubMed:24703693"
FT MOD_RES 207
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8C196"
FT MOD_RES 210
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8C196"
FT MOD_RES 210
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000269|PubMed:24703693"
FT MOD_RES 214
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8C196"
FT MOD_RES 214
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000269|PubMed:24703693"
FT MOD_RES 214
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8C196"
FT MOD_RES 219
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8C196"
FT MOD_RES 219
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000269|PubMed:24703693"
FT MOD_RES 228
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8C196"
FT MOD_RES 228
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000269|PubMed:24703693"
FT MOD_RES 237
FT /note="N6-glutaryllysine"
FT /evidence="ECO:0000269|PubMed:24703693"
FT MOD_RES 280
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8C196"
FT MOD_RES 280
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000269|PubMed:24703693"
FT MOD_RES 287
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8C196"
FT MOD_RES 287
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8C196"
FT MOD_RES 307
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8C196"
FT MOD_RES 307
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000269|PubMed:24703693"
FT MOD_RES 307
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8C196"
FT MOD_RES 310
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8C196"
FT MOD_RES 310
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000269|PubMed:24703693"
FT MOD_RES 400
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8C196"
FT MOD_RES 402
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000269|PubMed:24703693"
FT MOD_RES 402
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8C196"
FT MOD_RES 412
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8C196"
FT MOD_RES 412
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000269|PubMed:24703693"
FT MOD_RES 412
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8C196"
FT MOD_RES 453
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8C196"
FT MOD_RES 453
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000269|PubMed:24703693"
FT MOD_RES 458
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8C196"
FT MOD_RES 458
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000269|PubMed:24703693"
FT MOD_RES 458
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8C196"
FT MOD_RES 522
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8C196"
FT MOD_RES 522
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8C196"
FT MOD_RES 527
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8C196"
FT MOD_RES 527
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000269|PubMed:24703693"
FT MOD_RES 527
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8C196"
FT MOD_RES 532
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8C196"
FT MOD_RES 532
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000269|PubMed:24703693"
FT MOD_RES 537
FT /note="Phosphoserine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8C196"
FT MOD_RES 540
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P07756"
FT MOD_RES 553
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8C196"
FT MOD_RES 553
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000269|PubMed:24703693"
FT MOD_RES 553
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8C196"
FT MOD_RES 560
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8C196"
FT MOD_RES 560
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8C196"
FT MOD_RES 569
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 575
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8C196"
FT MOD_RES 575
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8C196"
FT MOD_RES 612
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8C196"
FT MOD_RES 612
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8C196"
FT MOD_RES 630
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8C196"
FT MOD_RES 728
FT /note="N6-glutaryllysine"
FT /evidence="ECO:0000269|PubMed:24703693"
FT MOD_RES 751
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8C196"
FT MOD_RES 751
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8C196"
FT MOD_RES 757
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8C196"
FT MOD_RES 757
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000269|PubMed:24703693"
FT MOD_RES 757
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8C196"
FT MOD_RES 772
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8C196"
FT MOD_RES 772
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000269|PubMed:24703693"
FT MOD_RES 793
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8C196"
FT MOD_RES 793
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000269|PubMed:24703693"
FT MOD_RES 793
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8C196"
FT MOD_RES 811
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8C196"
FT MOD_RES 811
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000269|PubMed:24703693"
FT MOD_RES 831
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8C196"
FT MOD_RES 831
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8C196"
FT MOD_RES 835
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 841
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8C196"
FT MOD_RES 841
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000269|PubMed:24703693"
FT MOD_RES 856
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8C196"
FT MOD_RES 856
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000269|PubMed:24703693"
FT MOD_RES 869
FT /note="N6-glutaryllysine"
FT /evidence="ECO:0000269|PubMed:24703693"
FT MOD_RES 875
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8C196"
FT MOD_RES 875
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000269|PubMed:24703693"
FT MOD_RES 875
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8C196"
FT MOD_RES 889
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8C196"
FT MOD_RES 889
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000269|PubMed:24703693"
FT MOD_RES 889
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8C196"
FT MOD_RES 892
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8C196"
FT MOD_RES 892
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000269|PubMed:24703693"
FT MOD_RES 892
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8C196"
FT MOD_RES 896
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P07756"
FT MOD_RES 898
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P07756"
FT MOD_RES 905
FT /note="N6-glutaryllysine"
FT /evidence="ECO:0000269|PubMed:24703693"
FT MOD_RES 908
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8C196"
FT MOD_RES 908
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000269|PubMed:24703693"
FT MOD_RES 915
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8C196"
FT MOD_RES 915
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000269|PubMed:24703693"
FT MOD_RES 915
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8C196"
FT MOD_RES 919
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8C196"
FT MOD_RES 919
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000269|PubMed:24703693"
FT MOD_RES 919
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8C196"
FT MOD_RES 935
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8C196"
FT MOD_RES 1036
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1074
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8C196"
FT MOD_RES 1074
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000269|PubMed:24703693"
FT MOD_RES 1074
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8C196"
FT MOD_RES 1079
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 1090
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P07756"
FT MOD_RES 1093
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P07756"
FT MOD_RES 1100
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8C196"
FT MOD_RES 1100
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8C196"
FT MOD_RES 1149
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8C196"
FT MOD_RES 1150
FT /note="N6-glutaryllysine"
FT /evidence="ECO:0000269|PubMed:24703693"
FT MOD_RES 1168
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8C196"
FT MOD_RES 1168
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000269|PubMed:24703693"
FT MOD_RES 1168
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8C196"
FT MOD_RES 1183
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8C196"
FT MOD_RES 1183
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000269|PubMed:24703693"
FT MOD_RES 1183
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8C196"
FT MOD_RES 1203
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1222
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8C196"
FT MOD_RES 1224
FT /note="N6-glutaryllysine"
FT /evidence="ECO:0000269|PubMed:24703693"
FT MOD_RES 1232
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8C196"
FT MOD_RES 1232
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8C196"
FT MOD_RES 1269
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8C196"
FT MOD_RES 1269
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8C196"
FT MOD_RES 1291
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8C196"
FT MOD_RES 1291
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8C196"
FT MOD_RES 1356
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8C196"
FT MOD_RES 1356
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000269|PubMed:24703693"
FT MOD_RES 1356
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8C196"
FT MOD_RES 1360
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000269|PubMed:24703693"
FT MOD_RES 1360
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8C196"
FT MOD_RES 1419
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1431
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1444
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8C196"
FT MOD_RES 1444
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8C196"
FT MOD_RES 1471
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8C196"
FT MOD_RES 1471
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8C196"
FT MOD_RES 1479
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8C196"
FT MOD_RES 1479
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000269|PubMed:24703693"
FT MOD_RES 1479
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8C196"
FT MOD_RES 1486
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8C196"
FT MOD_RES 1486
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000269|PubMed:24703693"
FT MOD_RES 1486
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8C196"
FT CARBOHYD 537
FT /note="O-linked (GlcNAc) serine; alternate"
FT /evidence="ECO:0000250"
FT CARBOHYD 1331
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 1332
FT /note="O-linked (GlcNAc) threonine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..451
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.4"
FT /id="VSP_009332"
FT VAR_SEQ 1
FT /note="M -> MPQIIKM (in isoform 3)"
FT /evidence="ECO:0000303|Ref.11"
FT /id="VSP_046685"
FT VARIANT 43
FT /note="A -> V (in CPS1D)"
FT /evidence="ECO:0000269|PubMed:21120950"
FT /id="VAR_066171"
FT VARIANT 58
FT /note="G -> D (in CPS1D)"
FT /evidence="ECO:0000269|PubMed:21120950"
FT /id="VAR_066172"
FT VARIANT 65
FT /note="S -> F (in CPS1D; dbSNP:rs375979196)"
FT /evidence="ECO:0000269|PubMed:21120950"
FT /id="VAR_066173"
FT VARIANT 71
FT /note="V -> G (in CPS1D)"
FT /evidence="ECO:0000269|PubMed:21120950"
FT /id="VAR_066174"
FT VARIANT 79
FT /note="G -> E (in CPS1D; dbSNP:rs1265394565)"
FT /evidence="ECO:0000269|PubMed:17310273"
FT /id="VAR_063560"
FT VARIANT 87
FT /note="P -> S (in CPS1D; dbSNP:rs1553509297)"
FT /evidence="ECO:0000269|PubMed:21120950"
FT /id="VAR_066175"
FT VARIANT 89
FT /note="Y -> D (in CPS1D)"
FT /evidence="ECO:0000269|PubMed:21120950"
FT /id="VAR_066176"
FT VARIANT 123
FT /note="S -> F (in CPS1D; modestly decreases enzyme
FT activity)"
FT /evidence="ECO:0000269|PubMed:20578160"
FT /id="VAR_064062"
FT VARIANT 123
FT /note="S -> Y (in CPS1D; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:26440671"
FT /id="VAR_075404"
FT VARIANT 165
FT /note="D -> G (in CPS1D)"
FT /evidence="ECO:0000269|PubMed:21120950"
FT /id="VAR_066177"
FT VARIANT 174
FT /note="R -> W (in CPS1D; unknown pathological significance;
FT dbSNP:rs1553509661)"
FT /evidence="ECO:0000269|PubMed:26440671"
FT /id="VAR_075405"
FT VARIANT 212
FT /note="Y -> N (in CPS1D)"
FT /evidence="ECO:0000269|PubMed:17310273"
FT /id="VAR_063561"
FT VARIANT 224
FT /note="D -> V (in CPS1D)"
FT /evidence="ECO:0000269|PubMed:21120950"
FT /id="VAR_066178"
FT VARIANT 233
FT /note="R -> C (in CPS1D; dbSNP:rs767905306)"
FT /evidence="ECO:0000269|PubMed:21120950"
FT /id="VAR_066179"
FT VARIANT 243
FT /note="H -> P (in CPS1D; dbSNP:rs752902711)"
FT /evidence="ECO:0000269|PubMed:21120950"
FT /id="VAR_066180"
FT VARIANT 258
FT /note="G -> E (in CPS1D)"
FT /evidence="ECO:0000269|PubMed:21120950"
FT /id="VAR_066181"
FT VARIANT 263
FT /note="G -> E (in CPS1D; dbSNP:rs1471393474)"
FT /evidence="ECO:0000269|PubMed:21120950"
FT /id="VAR_066182"
FT VARIANT 280
FT /note="K -> N (in CPS1D; dbSNP:rs753751183)"
FT /evidence="ECO:0000269|PubMed:17310273"
FT /id="VAR_063562"
FT VARIANT 301
FT /note="G -> E (in CPS1D; dbSNP:rs973321068)"
FT /evidence="ECO:0000269|PubMed:16737834"
FT /id="VAR_066104"
FT VARIANT 304
FT /note="A -> V (in CPS1D; associated with T-986;
FT dbSNP:rs775920437)"
FT /evidence="ECO:0000269|PubMed:21120950"
FT /id="VAR_066183"
FT VARIANT 317
FT /note="G -> E (in CPS1D; dbSNP:rs1273594946)"
FT /evidence="ECO:0000269|PubMed:21120950"
FT /id="VAR_066184"
FT VARIANT 337
FT /note="H -> R (in CPS1D; modestly decreases enzyme
FT activity; dbSNP:rs28940283)"
FT /evidence="ECO:0000269|PubMed:11474210,
FT ECO:0000269|PubMed:20578160"
FT /id="VAR_014077"
FT VARIANT 341
FT /note="L -> S (in CPS1D)"
FT /evidence="ECO:0000269|PubMed:22173106"
FT /id="VAR_075806"
FT VARIANT 344
FT /note="T -> A (no negative effect on protein stability,
FT enzyme activity and thermal stability; dbSNP:rs1047883)"
FT /evidence="ECO:0000269|PubMed:12853138,
FT ECO:0000269|PubMed:23649895, ECO:0000269|PubMed:9711878,
FT ECO:0000269|Ref.11"
FT /id="VAR_006834"
FT VARIANT 344
FT /note="T -> S (in dbSNP:rs1047883)"
FT /id="VAR_061752"
FT VARIANT 355
FT /note="N -> D (in CPS1D; around 80% decrease in enzyme
FT activity; significant reduction in thermal stability;
FT approximately 4-fold decrease in the apparent Vmax for ATP,
FT bicarbonate and ammonia; dbSNP:rs1472190012)"
FT /evidence="ECO:0000269|PubMed:23649895"
FT /id="VAR_075406"
FT VARIANT 358
FT /note="D -> H (in CPS1D; dbSNP:rs149930500)"
FT /evidence="ECO:0000269|PubMed:21120950"
FT /id="VAR_066185"
FT VARIANT 382
FT /note="P -> L (in CPS1D; dbSNP:rs201407486)"
FT /evidence="ECO:0000269|PubMed:21120950"
FT /id="VAR_066186"
FT VARIANT 389
FT /note="Y -> C (in CPS1D; around 40% decrease in enzyme
FT activity; significant loss of thermal stability)"
FT /evidence="ECO:0000269|PubMed:16737834,
FT ECO:0000269|PubMed:23649895"
FT /id="VAR_066105"
FT VARIANT 390
FT /note="L -> R (in CPS1D; significant loss of protein
FT stability)"
FT /evidence="ECO:0000269|PubMed:16737834,
FT ECO:0000269|PubMed:23649895"
FT /id="VAR_066106"
FT VARIANT 401
FT /note="G -> R (in CPS1D; unknown pathological significance;
FT associated with N-937 in a patient; dbSNP:rs760895692)"
FT /evidence="ECO:0000269|PubMed:21120950,
FT ECO:0000269|PubMed:24813853"
FT /id="VAR_066187"
FT VARIANT 431
FT /note="G -> R (in CPS1D; dbSNP:rs778766382)"
FT /evidence="ECO:0000269|PubMed:21120950"
FT /id="VAR_066188"
FT VARIANT 432
FT /note="G -> V (in CPS1D)"
FT /evidence="ECO:0000269|PubMed:21120950"
FT /id="VAR_066189"
FT VARIANT 438
FT /note="A -> P (in CPS1D; almost complete loss of enzyme
FT activity; dbSNP:rs772497399)"
FT /evidence="ECO:0000269|PubMed:17310273,
FT ECO:0000269|PubMed:23649895"
FT /id="VAR_063563"
FT VARIANT 438
FT /note="A -> T (in CPS1D; dbSNP:rs772497399)"
FT /evidence="ECO:0000269|PubMed:21120950"
FT /id="VAR_066190"
FT VARIANT 450
FT /note="K -> E (in CPS1D)"
FT /evidence="ECO:0000269|PubMed:21120950"
FT /id="VAR_066191"
FT VARIANT 457
FT /note="V -> G (in CPS1D; dbSNP:rs371350538)"
FT /evidence="ECO:0000269|PubMed:12955727"
FT /id="VAR_017562"
FT VARIANT 471
FT /note="T -> N (in CPS1D)"
FT /evidence="ECO:0000269|PubMed:20578160"
FT /id="VAR_064063"
FT VARIANT 498
FT /note="A -> P (in CPS1D)"
FT /evidence="ECO:0000269|PubMed:21120950"
FT /id="VAR_066192"
FT VARIANT 530
FT /note="G -> V (found in a patient with VACTERL syndrome and
FT postsurgical PHN; unknown pathological significance;
FT dbSNP:rs1250316045)"
FT /evidence="ECO:0000269|PubMed:21767969"
FT /id="VAR_070211"
FT VARIANT 531
FT /note="V -> E (in CPS1D)"
FT /evidence="ECO:0000269|PubMed:21120950"
FT /id="VAR_066193"
FT VARIANT 531
FT /note="V -> G (in CPS1D)"
FT /evidence="ECO:0000269|PubMed:21120950"
FT /id="VAR_066194"
FT VARIANT 544
FT /note="T -> M (in CPS1D; almost complete loss of enzyme
FT activity; approximately 60-fold increase in the apparent Km
FT for bicarbonate and approximately 4-fold respective
FT decrease and increase in the apparent Vmax and Km for
FT ammonia; dbSNP:rs121912592)"
FT /evidence="ECO:0000269|PubMed:21120950,
FT ECO:0000269|PubMed:23649895, ECO:0000269|PubMed:9711878"
FT /id="VAR_006835"
FT VARIANT 587
FT /note="R -> C (in CPS1D; dbSNP:rs1242028775)"
FT /evidence="ECO:0000269|PubMed:21120950"
FT /id="VAR_066195"
FT VARIANT 587
FT /note="R -> H (in CPS1D; dbSNP:rs1553512642)"
FT /evidence="ECO:0000269|PubMed:17310273,
FT ECO:0000269|PubMed:21120950"
FT /id="VAR_063564"
FT VARIANT 587
FT /note="R -> L (in CPS1D)"
FT /evidence="ECO:0000269|PubMed:21120950"
FT /id="VAR_066196"
FT VARIANT 589
FT /note="A -> T (in CPS1D; dbSNP:rs777233486)"
FT /evidence="ECO:0000269|PubMed:16737834"
FT /id="VAR_066142"
FT VARIANT 593
FT /note="G -> R (in CPS1D; dbSNP:rs1048119191)"
FT /evidence="ECO:0000269|PubMed:17310273"
FT /id="VAR_063565"
FT VARIANT 597
FT /note="S -> L (in CPS1D)"
FT /evidence="ECO:0000269|PubMed:21120950"
FT /id="VAR_066197"
FT VARIANT 622
FT /note="V -> M (in CPS1D; dbSNP:rs1553512962)"
FT /evidence="ECO:0000269|PubMed:21120950"
FT /id="VAR_066198"
FT VARIANT 628
FT /note="G -> D (in CPS1D; dbSNP:rs1275599086)"
FT /evidence="ECO:0000269|PubMed:21120950"
FT /id="VAR_066199"
FT VARIANT 632
FT /note="I -> R (in CPS1D; dbSNP:rs1553512974)"
FT /evidence="ECO:0000269|PubMed:21120950,
FT ECO:0000269|PubMed:24813853"
FT /id="VAR_066200"
FT VARIANT 638
FT /note="R -> P (in CPS1D; dbSNP:rs757205958)"
FT /evidence="ECO:0000269|PubMed:21120950"
FT /id="VAR_066201"
FT VARIANT 640
FT /note="A -> S (in CPS1D; dbSNP:rs142693704)"
FT /evidence="ECO:0000269|PubMed:16737834"
FT /id="VAR_066143"
FT VARIANT 648
FT /note="C -> Y (in CPS1D)"
FT /evidence="ECO:0000269|PubMed:21120950"
FT /id="VAR_066202"
FT VARIANT 651
FT /note="E -> K (in CPS1D)"
FT /evidence="ECO:0000269|PubMed:17310273"
FT /id="VAR_063566"
FT VARIANT 654
FT /note="D -> V (in CPS1D)"
FT /evidence="ECO:0000269|PubMed:21120950"
FT /id="VAR_066203"
FT VARIANT 661
FT /note="G -> R (in CPS1D)"
FT /evidence="ECO:0000269|PubMed:22173106"
FT /id="VAR_075807"
FT VARIANT 674
FT /note="N -> I (in CPS1D)"
FT /evidence="ECO:0000269|PubMed:17310273"
FT /id="VAR_063567"
FT VARIANT 674
FT /note="N -> K (in CPS1D; dbSNP:rs1248368809)"
FT /evidence="ECO:0000269|PubMed:21120950"
FT /id="VAR_066204"
FT VARIANT 678
FT /note="Q -> P (in CPS1D; results in a poor enzyme
FT expression and solubility; hampers correct enzyme folding)"
FT /evidence="ECO:0000269|PubMed:20578160"
FT /id="VAR_064064"
FT VARIANT 698
FT /note="N -> S (in CPS1D)"
FT /evidence="ECO:0000269|PubMed:21120950"
FT /id="VAR_066205"
FT VARIANT 716
FT /note="N -> K (in CPS1D; dbSNP:rs369061090)"
FT /evidence="ECO:0000269|PubMed:16737834"
FT /id="VAR_066144"
FT VARIANT 718
FT /note="R -> K (in CPS1D)"
FT /evidence="ECO:0000269|PubMed:21120950"
FT /id="VAR_066107"
FT VARIANT 721
FT /note="R -> Q (in CPS1D; dbSNP:rs752339705)"
FT /evidence="ECO:0000269|PubMed:21120950"
FT /id="VAR_066108"
FT VARIANT 724
FT /note="A -> P (in CPS1D)"
FT /evidence="ECO:0000269|PubMed:21120950"
FT /id="VAR_066109"
FT VARIANT 726
FT /note="A -> T (in CPS1D)"
FT /evidence="ECO:0000269|PubMed:21120950"
FT /id="VAR_066110"
FT VARIANT 767
FT /note="D -> V (in CPS1D)"
FT /evidence="ECO:0000269|PubMed:21120950"
FT /id="VAR_066111"
FT VARIANT 774
FT /note="P -> L (in CPS1D; the enzyme is inactive)"
FT /evidence="ECO:0000269|PubMed:20578160"
FT /id="VAR_064065"
FT VARIANT 780
FT /note="R -> H (in CPS1D; dbSNP:rs758724746)"
FT /evidence="ECO:0000269|PubMed:17310273,
FT ECO:0000269|PubMed:21120950"
FT /id="VAR_063568"
FT VARIANT 792
FT /note="M -> I (in CPS1D; dbSNP:rs1553513429)"
FT /evidence="ECO:0000269|PubMed:21120950"
FT /id="VAR_066112"
FT VARIANT 803
FT /note="R -> C (in CPS1D; dbSNP:rs201716417)"
FT /evidence="ECO:0000269|PubMed:21120950"
FT /id="VAR_066145"
FT VARIANT 803
FT /note="R -> G (in CPS1D; dbSNP:rs201716417)"
FT /evidence="ECO:0000269|PubMed:21120950,
FT ECO:0000269|PubMed:26440671"
FT /id="VAR_066146"
FT VARIANT 803
FT /note="R -> S (in CPS1D; dbSNP:rs201716417)"
FT /evidence="ECO:0000269|PubMed:21120950"
FT /id="VAR_066147"
FT VARIANT 805
FT /note="F -> L (in CPS1D; dbSNP:rs1553513861)"
FT /evidence="ECO:0000269|PubMed:16737834"
FT /id="VAR_066148"
FT VARIANT 805
FT /note="F -> S (in CPS1D)"
FT /evidence="ECO:0000269|PubMed:21120950"
FT /id="VAR_066149"
FT VARIANT 810
FT /note="Q -> R (in CPS1D; dbSNP:rs1553513864)"
FT /evidence="ECO:0000269|PubMed:12955727"
FT /id="VAR_017563"
FT VARIANT 814
FT /note="R -> W (in CPS1D; dbSNP:rs772782772)"
FT /evidence="ECO:0000269|PubMed:21120950"
FT /id="VAR_066150"
FT VARIANT 816
FT /note="C -> R (in CPS1D; dbSNP:rs1553513870)"
FT /evidence="ECO:0000269|PubMed:21120950"
FT /id="VAR_066151"
FT VARIANT 843
FT /note="L -> S (in CPS1D; associated in cis with E-875;
FT causes 70% decrease of enzyme activity; significant
FT decrease in protein yield)"
FT /evidence="ECO:0000269|PubMed:12655559,
FT ECO:0000269|PubMed:15164414, ECO:0000269|PubMed:24813853"
FT /id="VAR_017564"
FT VARIANT 850
FT /note="R -> C (in CPS1D; moderate decrease in protein yield
FT and partial loss of enzyme activity; dbSNP:rs1015051007)"
FT /evidence="ECO:0000269|PubMed:17310273,
FT ECO:0000269|PubMed:24813853"
FT /id="VAR_063569"
FT VARIANT 850
FT /note="R -> H (in CPS1D; partial loss of enzyme activity;
FT dbSNP:rs767694281)"
FT /evidence="ECO:0000269|PubMed:15617192,
FT ECO:0000269|PubMed:21120950, ECO:0000269|PubMed:24813853,
FT ECO:0000269|PubMed:26440671"
FT /id="VAR_030675"
FT VARIANT 871
FT /note="T -> P (in CPS1D; significant decrease in protein
FT yield and enzyme activity)"
FT /evidence="ECO:0000269|PubMed:24813853"
FT /id="VAR_075407"
FT VARIANT 875
FT /note="K -> E (associated in cis with S-843 in a patient
FT with carbamoyl-phosphate synthase deficiency; does not
FT affect enzyme activity; significant decrease in protein
FT yield and thermal stability; dbSNP:rs147062907)"
FT /evidence="ECO:0000269|PubMed:12655559,
FT ECO:0000269|PubMed:15164414, ECO:0000269|PubMed:24813853,
FT ECO:0000269|PubMed:27535533"
FT /id="VAR_017565"
FT VARIANT 911
FT /note="G -> E (in CPS1D; significant decrease in protein
FT yield and enzyme activity; dbSNP:rs1388955593)"
FT /evidence="ECO:0000269|PubMed:21120950,
FT ECO:0000269|PubMed:24813853"
FT /id="VAR_066152"
FT VARIANT 911
FT /note="G -> V (in CPS1D; significant decrease in protein
FT yield and enzyme activity)"
FT /evidence="ECO:0000269|PubMed:16737834,
FT ECO:0000269|PubMed:24813853"
FT /id="VAR_066153"
FT VARIANT 913
FT /note="S -> L (in CPS1D; significant decrease in protein
FT yield and partial loss of enzyme activity;
FT dbSNP:rs754706559)"
FT /evidence="ECO:0000269|PubMed:21120950,
FT ECO:0000269|PubMed:24813853"
FT /id="VAR_066154"
FT VARIANT 914
FT /note="D -> G (in CPS1D; significant decrease in protein
FT yield and enzyme activity)"
FT /evidence="ECO:0000269|PubMed:21120950,
FT ECO:0000269|PubMed:24813853"
FT /id="VAR_066155"
FT VARIANT 914
FT /note="D -> H (in CPS1D; significant decrease in protein
FT yield and enzyme activity; dbSNP:rs765484849)"
FT /evidence="ECO:0000269|PubMed:21120950,
FT ECO:0000269|PubMed:24813853"
FT /id="VAR_066156"
FT VARIANT 918
FT /note="S -> P (in CPS1D; significant decrease in protein
FT yield and enzyme activity)"
FT /evidence="ECO:0000269|PubMed:15617192,
FT ECO:0000269|PubMed:24813853"
FT /id="VAR_030676"
FT VARIANT 932
FT /note="R -> T (in CPS1D; significant decrease in protein
FT yield and partial loss of enzyme activity)"
FT /evidence="ECO:0000269|PubMed:21120950,
FT ECO:0000269|PubMed:24813853"
FT /id="VAR_066157"
FT VARIANT 937
FT /note="I -> N (in CPS1D; associated with R-401; significant
FT decrease in protein yield and enzyme activity;
FT dbSNP:rs760714614)"
FT /evidence="ECO:0000269|PubMed:24813853"
FT /id="VAR_075408"
FT VARIANT 949
FT /note="A -> T (in CPS1D; partial loss of enzyme activity
FT and significant decrease in thermal stability;
FT dbSNP:rs537170841)"
FT /evidence="ECO:0000269|PubMed:21120950,
FT ECO:0000269|PubMed:24813853"
FT /id="VAR_066158"
FT VARIANT 958
FT /note="L -> P (in CPS1D; significant decrease in protein
FT yield and enzyme activity)"
FT /evidence="ECO:0000269|PubMed:16737834,
FT ECO:0000269|PubMed:24813853"
FT /id="VAR_066159"
FT VARIANT 959
FT /note="Y -> C (in CPS1D; significant decrease in protein
FT yield and thermal stability; partial loss of enzyme
FT activity; dbSNP:rs1191587211)"
FT /evidence="ECO:0000269|PubMed:21120950,
FT ECO:0000269|PubMed:24813853"
FT /id="VAR_066160"
FT VARIANT 962
FT /note="Y -> C (in CPS1D; significant decrease in protein
FT yield and partial loss of enzyme activity;
FT dbSNP:rs955666400)"
FT /evidence="ECO:0000269|PubMed:21120950,
FT ECO:0000269|PubMed:24813853"
FT /id="VAR_066161"
FT VARIANT 964
FT /note="G -> D (in CPS1D; significant decrease in protein
FT yield and enzyme activity; dbSNP:rs534815243)"
FT /evidence="ECO:0000269|PubMed:22173106,
FT ECO:0000269|PubMed:24813853"
FT /id="VAR_075409"
FT VARIANT 978
FT /note="V -> E (in CPS1D)"
FT /evidence="ECO:0000269|PubMed:21120950"
FT /id="VAR_066113"
FT VARIANT 982
FT /note="G -> D (in CPS1D; dbSNP:rs121912595)"
FT /evidence="ECO:0000269|PubMed:17310273"
FT /id="VAR_063570"
FT VARIANT 982
FT /note="G -> S (in CPS1D; dbSNP:rs757059355)"
FT /evidence="ECO:0000269|PubMed:16737834"
FT /id="VAR_066162"
FT VARIANT 982
FT /note="G -> V (in CPS1D; dbSNP:rs121912595)"
FT /evidence="ECO:0000269|PubMed:21120950"
FT /id="VAR_066114"
FT VARIANT 984
FT /note="Y -> H (in CPS1D)"
FT /evidence="ECO:0000269|PubMed:21120950"
FT /id="VAR_066115"
FT VARIANT 986
FT /note="I -> T (in CPS1D; associated with V-304;
FT dbSNP:rs1553516442)"
FT /evidence="ECO:0000269|PubMed:21120950"
FT /id="VAR_066116"
FT VARIANT 987
FT /note="G -> C (in CPS1D; may affect splicing;
FT dbSNP:rs1553516443)"
FT /evidence="ECO:0000269|PubMed:21120950"
FT /id="VAR_066117"
FT VARIANT 992
FT /note="F -> S (in CPS1D; dbSNP:rs990390709)"
FT /evidence="ECO:0000269|PubMed:21120950"
FT /id="VAR_066118"
FT VARIANT 998
FT /note="S -> F (in CPS1D; dbSNP:rs1404696893)"
FT /evidence="ECO:0000269|PubMed:16737834"
FT /id="VAR_066163"
FT VARIANT 1016
FT /note="N -> S (in CPS1D; dbSNP:rs749238466)"
FT /evidence="ECO:0000269|PubMed:21120950"
FT /id="VAR_066119"
FT VARIANT 1017
FT /note="P -> L (in CPS1D)"
FT /evidence="ECO:0000269|PubMed:21120950"
FT /id="VAR_066120"
FT VARIANT 1022
FT /note="T -> I (in CPS1D; dbSNP:rs1437651658)"
FT /evidence="ECO:0000269|PubMed:21120950"
FT /id="VAR_066121"
FT VARIANT 1034
FT /note="E -> G (in CPS1D)"
FT /evidence="ECO:0000269|PubMed:21120950"
FT /id="VAR_066122"
FT VARIANT 1045
FT /note="H -> R (in CPS1D; dbSNP:rs1241423400)"
FT /evidence="ECO:0000269|PubMed:21120950"
FT /id="VAR_066123"
FT VARIANT 1054
FT /note="I -> R (in CPS1D)"
FT /evidence="ECO:0000269|PubMed:11388595"
FT /id="VAR_066164"
FT VARIANT 1059
FT /note="Q -> R (in CPS1D)"
FT /evidence="ECO:0000269|PubMed:21120950"
FT /id="VAR_066124"
FT VARIANT 1065
FT /note="A -> E (in CPS1D; dbSNP:rs770471782)"
FT /evidence="ECO:0000269|PubMed:21120950"
FT /id="VAR_066125"
FT VARIANT 1089
FT /note="R -> C (in CPS1D; dbSNP:rs1392559810)"
FT /evidence="ECO:0000269|PubMed:21120950"
FT /id="VAR_066126"
FT VARIANT 1089
FT /note="R -> L (in CPS1D; dbSNP:rs1280211937)"
FT /evidence="ECO:0000269|PubMed:16737834"
FT /id="VAR_066165"
FT VARIANT 1103
FT /note="Q -> R (in CPS1D)"
FT /evidence="ECO:0000269|PubMed:17310273"
FT /id="VAR_063571"
FT VARIANT 1141
FT /note="V -> G (in CPS1D)"
FT /evidence="ECO:0000269|PubMed:17310273"
FT /id="VAR_063572"
FT VARIANT 1155
FT /note="A -> E (in CPS1D)"
FT /evidence="ECO:0000269|PubMed:21120950"
FT /id="VAR_066127"
FT VARIANT 1155
FT /note="A -> V (in CPS1D; dbSNP:rs766125631)"
FT /evidence="ECO:0000269|PubMed:21120950"
FT /id="VAR_066128"
FT VARIANT 1167
FT /note="T -> R (in CPS1D)"
FT /evidence="ECO:0000269|PubMed:22173106"
FT /id="VAR_075808"
FT VARIANT 1194
FT /note="E -> D (in CPS1D)"
FT /evidence="ECO:0000269|PubMed:24813853"
FT /id="VAR_075410"
FT VARIANT 1195
FT /note="H -> P (in CPS1D)"
FT /evidence="ECO:0000269|PubMed:17310273"
FT /id="VAR_063573"
FT VARIANT 1203
FT /note="S -> L (in CPS1D; dbSNP:rs149518280)"
FT /evidence="ECO:0000269|PubMed:21120950"
FT /id="VAR_066129"
FT VARIANT 1203
FT /note="S -> P (in CPS1D; dbSNP:rs1319489001)"
FT /evidence="ECO:0000269|PubMed:16737834"
FT /id="VAR_066166"
FT VARIANT 1205
FT /note="D -> N (in CPS1D)"
FT /evidence="ECO:0000269|PubMed:16737834"
FT /id="VAR_066167"
FT VARIANT 1215
FT /note="I -> V (in CPS1D; unknown pathological significance;
FT dbSNP:rs141373204)"
FT /evidence="ECO:0000269|PubMed:17310273"
FT /id="VAR_063574"
FT VARIANT 1228
FT /note="R -> Q (in CPS1D; dbSNP:rs778117194)"
FT /evidence="ECO:0000269|PubMed:21120950"
FT /id="VAR_066130"
FT VARIANT 1241
FT /note="N -> K (in CPS1D)"
FT /evidence="ECO:0000269|PubMed:17310273"
FT /id="VAR_063575"
FT VARIANT 1254
FT /note="I -> F (in CPS1D; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:26440671"
FT /id="VAR_075411"
FT VARIANT 1255
FT /note="E -> D (in CPS1D)"
FT /evidence="ECO:0000269|PubMed:21120950"
FT /id="VAR_066131"
FT VARIANT 1262
FT /note="R -> P (in CPS1D)"
FT /evidence="ECO:0000269|PubMed:21120950"
FT /id="VAR_066132"
FT VARIANT 1262
FT /note="R -> Q (in CPS1D; dbSNP:rs750670270)"
FT /evidence="ECO:0000269|PubMed:21120950"
FT /id="VAR_066133"
FT VARIANT 1266
FT /note="F -> S (in dbSNP:rs1047886)"
FT /evidence="ECO:0000269|PubMed:1840546"
FT /id="VAR_017566"
FT VARIANT 1274
FT /note="D -> H (in CPS1D)"
FT /evidence="ECO:0000269|PubMed:21120950"
FT /id="VAR_066134"
FT VARIANT 1283
FT /note="M -> L (in dbSNP:rs1047887)"
FT /evidence="ECO:0000269|PubMed:1840546"
FT /id="VAR_017567"
FT VARIANT 1327
FT /note="C -> R (in CPS1D)"
FT /evidence="ECO:0000269|PubMed:21120950"
FT /id="VAR_066135"
FT VARIANT 1331
FT /note="S -> P (in CPS1D)"
FT /evidence="ECO:0000269|PubMed:16737834"
FT /id="VAR_066168"
FT VARIANT 1333
FT /note="G -> E (in CPS1D; dbSNP:rs372645328)"
FT /evidence="ECO:0000269|PubMed:21120950"
FT /id="VAR_066136"
FT VARIANT 1363..1366
FT /note="Missing (in CPS1D; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:26440671"
FT /id="VAR_075412"
FT VARIANT 1371
FT /note="R -> L (in CPS1D)"
FT /evidence="ECO:0000269|PubMed:21120950"
FT /id="VAR_066137"
FT VARIANT 1376
FT /note="G -> S (no functional consequences; no negative
FT effect on protein stability, enzyme activity and thermal
FT stability; dbSNP:rs140578009)"
FT /evidence="ECO:0000269|PubMed:12853138,
FT ECO:0000269|PubMed:20578160, ECO:0000269|PubMed:23649895"
FT /id="VAR_017568"
FT VARIANT 1378
FT /note="A -> T (in CPS1D; significant reduction in thermal
FT stability; dbSNP:rs1245373037)"
FT /evidence="ECO:0000269|PubMed:16737834,
FT ECO:0000269|PubMed:23649895"
FT /id="VAR_066169"
FT VARIANT 1381
FT /note="L -> S (in CPS1D; significant loss of protein
FT stability)"
FT /evidence="ECO:0000269|PubMed:23649895"
FT /id="VAR_075413"
FT VARIANT 1391
FT /note="T -> M (in CPS1D; dbSNP:rs1392934477)"
FT /evidence="ECO:0000269|PubMed:21120950"
FT /id="VAR_066138"
FT VARIANT 1398
FT /note="L -> V (in CPS1D)"
FT /evidence="ECO:0000269|PubMed:21120950"
FT /id="VAR_066139"
FT VARIANT 1406
FT /note="T -> N (associated with susceptibility to neonatal
FT pulmonary hypertension; also highly associated with
FT hepatocellular carcinoma progression; dbSNP:rs1047891)"
FT /evidence="ECO:0000269|PubMed:11407344,
FT ECO:0000269|PubMed:12853138, ECO:0000269|PubMed:12955727,
FT ECO:0000269|PubMed:1840546, ECO:0000269|PubMed:20520828,
FT ECO:0000269|PubMed:21767969, ECO:0000269|PubMed:24237036"
FT /id="VAR_017569"
FT VARIANT 1411
FT /note="P -> L (in CPS1D; modestly decreases enzyme
FT activity; dbSNP:rs1202306773)"
FT /evidence="ECO:0000269|PubMed:16737834,
FT ECO:0000269|PubMed:20578160"
FT /id="VAR_064066"
FT VARIANT 1439
FT /note="P -> L (in CPS1D)"
FT /evidence="ECO:0000269|PubMed:21120950"
FT /id="VAR_066140"
FT VARIANT 1443
FT /note="T -> A (in CPS1D; almost complete loss of enzyme
FT activity; approximately 10-fold decrease in the apparent
FT Vmax for bicarbonate, ammonia and ATP; decreased affinity
FT for NAG)"
FT /evidence="ECO:0000269|PubMed:16737834,
FT ECO:0000269|PubMed:23649895"
FT /id="VAR_066170"
FT VARIANT 1453
FT /note="R -> Q (in CPS1D; the enzyme is inactive)"
FT /evidence="ECO:0000269|PubMed:20578160"
FT /id="VAR_064067"
FT VARIANT 1453
FT /note="R -> W (in CPS1D; the enzyme is inactive;
FT dbSNP:rs933813349)"
FT /evidence="ECO:0000269|PubMed:20578160,
FT ECO:0000269|PubMed:21120950"
FT /id="VAR_064068"
FT VARIANT 1462
FT /note="P -> R (in CPS1D)"
FT /evidence="ECO:0000269|PubMed:21120950,
FT ECO:0000269|PubMed:24813853"
FT /id="VAR_066141"
FT VARIANT 1491
FT /note="Y -> H (in CPS1D; triggers a large decrease in the
FT apparent affinity for N-acetyl-L-glutamate (NAG);
FT dbSNP:rs1553519513)"
FT /evidence="ECO:0000269|PubMed:20578160"
FT /id="VAR_064069"
FT CONFLICT 111
FT /note="A -> S (in Ref. 1; BAA14328)"
FT /evidence="ECO:0000305"
FT CONFLICT 279
FT /note="R -> Q (in Ref. 1; BAA14328)"
FT /evidence="ECO:0000305"
FT CONFLICT 338
FT /note="G -> C (in Ref. 1; BAA14328)"
FT /evidence="ECO:0000305"
FT CONFLICT 718..722
FT /note="RLSRS -> KMSPN (in Ref. 1; BAA14328)"
FT /evidence="ECO:0000305"
FT CONFLICT 729
FT /note="A -> T (in Ref. 1; BAA14328)"
FT /evidence="ECO:0000305"
FT CONFLICT 749
FT /note="E -> G (in Ref. 1; BAA14328)"
FT /evidence="ECO:0000305"
FT CONFLICT 912
FT /note="F -> L (in Ref. 6; CAE45707)"
FT /evidence="ECO:0000305"
FT CONFLICT 1161..1162
FT /note="EH -> AT (in Ref. 1; BAA14328)"
FT /evidence="ECO:0000305"
FT CONFLICT 1204..1205
FT /note="GD -> EN (in Ref. 1; BAA14328)"
FT /evidence="ECO:0000305"
FT CONFLICT 1254
FT /note="I -> N (in Ref. 1; BAA14328)"
FT /evidence="ECO:0000305"
FT CONFLICT 1303
FT /note="A -> V (in Ref. 1; BAA14328)"
FT /evidence="ECO:0000305"
FT STRAND 45..50
FT /evidence="ECO:0007829|PDB:6UEL"
FT STRAND 55..60
FT /evidence="ECO:0007829|PDB:6UEL"
FT STRAND 67..74
FT /evidence="ECO:0007829|PDB:6UEL"
FT HELIX 80..84
FT /evidence="ECO:0007829|PDB:6UEL"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:6UEL"
FT STRAND 92..101
FT /evidence="ECO:0007829|PDB:6UEL"
FT STRAND 116..120
FT /evidence="ECO:0007829|PDB:6UEL"
FT STRAND 122..125
FT /evidence="ECO:0007829|PDB:6UEL"
FT STRAND 128..132
FT /evidence="ECO:0007829|PDB:6UEL"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:6UEL"
FT HELIX 149..155
FT /evidence="ECO:0007829|PDB:6UEL"
FT STRAND 160..163
FT /evidence="ECO:0007829|PDB:6UEL"
FT HELIX 166..173
FT /evidence="ECO:0007829|PDB:6UEL"
FT STRAND 179..184
FT /evidence="ECO:0007829|PDB:6UEL"
FT HELIX 195..197
FT /evidence="ECO:0007829|PDB:6UEL"
FT HELIX 200..204
FT /evidence="ECO:0007829|PDB:6UEL"
FT STRAND 210..213
FT /evidence="ECO:0007829|PDB:6UEL"
FT STRAND 217..226
FT /evidence="ECO:0007829|PDB:6UEL"
FT HELIX 229..237
FT /evidence="ECO:0007829|PDB:6UEL"
FT STRAND 240..245
FT /evidence="ECO:0007829|PDB:6UEL"
FT STRAND 257..263
FT /evidence="ECO:0007829|PDB:6UEL"
FT HELIX 268..270
FT /evidence="ECO:0007829|PDB:6UEL"
FT HELIX 272..283
FT /evidence="ECO:0007829|PDB:6UEL"
FT STRAND 290..294
FT /evidence="ECO:0007829|PDB:6UEL"
FT HELIX 295..304
FT /evidence="ECO:0007829|PDB:6UEL"
FT STRAND 308..324
FT /evidence="ECO:0007829|PDB:6UEL"
FT TURN 325..327
FT /evidence="ECO:0007829|PDB:6UEL"
FT STRAND 330..341
FT /evidence="ECO:0007829|PDB:6UEL"
FT STRAND 349..351
FT /evidence="ECO:0007829|PDB:6UEL"
FT STRAND 353..355
FT /evidence="ECO:0007829|PDB:6UEL"
FT TURN 356..358
FT /evidence="ECO:0007829|PDB:6UEL"
FT STRAND 363..376
FT /evidence="ECO:0007829|PDB:6UEL"
FT STRAND 381..383
FT /evidence="ECO:0007829|PDB:6UEL"
FT HELIX 389..399
FT /evidence="ECO:0007829|PDB:6UEL"
FT HELIX 405..408
FT /evidence="ECO:0007829|PDB:6UEL"
FT STRAND 423..428
FT /evidence="ECO:0007829|PDB:6UEL"
FT STRAND 435..437
FT /evidence="ECO:0007829|PDB:5DOT"
FT HELIX 445..454
FT /evidence="ECO:0007829|PDB:6UEL"
FT STRAND 458..462
FT /evidence="ECO:0007829|PDB:6UEL"
FT HELIX 469..471
FT /evidence="ECO:0007829|PDB:6UEL"
FT STRAND 473..475
FT /evidence="ECO:0007829|PDB:5DOU"
FT STRAND 480..483
FT /evidence="ECO:0007829|PDB:6UEL"
FT HELIX 489..499
FT /evidence="ECO:0007829|PDB:6UEL"
FT STRAND 502..505
FT /evidence="ECO:0007829|PDB:6UEL"
FT STRAND 507..509
FT /evidence="ECO:0007829|PDB:6UEL"
FT HELIX 510..522
FT /evidence="ECO:0007829|PDB:6UEL"
FT HELIX 525..529
FT /evidence="ECO:0007829|PDB:6UEL"
FT HELIX 538..545
FT /evidence="ECO:0007829|PDB:6UEL"
FT HELIX 547..555
FT /evidence="ECO:0007829|PDB:6UEL"
FT TURN 556..558
FT /evidence="ECO:0007829|PDB:6UEL"
FT STRAND 563..569
FT /evidence="ECO:0007829|PDB:5DOU"
FT HELIX 570..580
FT /evidence="ECO:0007829|PDB:5DOU"
FT STRAND 582..590
FT /evidence="ECO:0007829|PDB:5DOU"
FT TURN 593..596
FT /evidence="ECO:0007829|PDB:5DOU"
FT STRAND 598..602
FT /evidence="ECO:0007829|PDB:5DOU"
FT HELIX 603..614
FT /evidence="ECO:0007829|PDB:5DOU"
FT STRAND 620..624
FT /evidence="ECO:0007829|PDB:5DOU"
FT STRAND 629..638
FT /evidence="ECO:0007829|PDB:6UEL"
FT STRAND 644..655
FT /evidence="ECO:0007829|PDB:6UEL"
FT HELIX 660..662
FT /evidence="ECO:0007829|PDB:5DOU"
FT STRAND 663..668
FT /evidence="ECO:0007829|PDB:6UEL"
FT HELIX 674..690
FT /evidence="ECO:0007829|PDB:6UEL"
FT STRAND 695..703
FT /evidence="ECO:0007829|PDB:6UEL"
FT STRAND 710..716
FT /evidence="ECO:0007829|PDB:6UEL"
FT HELIX 721..730
FT /evidence="ECO:0007829|PDB:6UEL"
FT HELIX 734..742
FT /evidence="ECO:0007829|PDB:6UEL"
FT HELIX 747..749
FT /evidence="ECO:0007829|PDB:6UEL"
FT TURN 753..755
FT /evidence="ECO:0007829|PDB:6UEL"
FT STRAND 756..762
FT /evidence="ECO:0007829|PDB:6UEL"
FT STRAND 767..777
FT /evidence="ECO:0007829|PDB:6UEL"
FT STRAND 794..804
FT /evidence="ECO:0007829|PDB:6UEL"
FT HELIX 805..816
FT /evidence="ECO:0007829|PDB:6UEL"
FT HELIX 828..830
FT /evidence="ECO:0007829|PDB:5DOT"
FT HELIX 839..844
FT /evidence="ECO:0007829|PDB:6UEL"
FT HELIX 850..859
FT /evidence="ECO:0007829|PDB:6UEL"
FT HELIX 864..871
FT /evidence="ECO:0007829|PDB:6UEL"
FT HELIX 875..892
FT /evidence="ECO:0007829|PDB:6UEL"
FT TURN 896..898
FT /evidence="ECO:0007829|PDB:6UEL"
FT HELIX 901..909
FT /evidence="ECO:0007829|PDB:6UEL"
FT HELIX 914..921
FT /evidence="ECO:0007829|PDB:6UEL"
FT HELIX 925..934
FT /evidence="ECO:0007829|PDB:6UEL"
FT STRAND 940..943
FT /evidence="ECO:0007829|PDB:6UEL"
FT STRAND 957..963
FT /evidence="ECO:0007829|PDB:6UEL"
FT STRAND 976..979
FT /evidence="ECO:0007829|PDB:6UEL"
FT HELIX 991..1005
FT /evidence="ECO:0007829|PDB:6UEL"
FT STRAND 1010..1014
FT /evidence="ECO:0007829|PDB:6UEL"
FT TURN 1024..1026
FT /evidence="ECO:0007829|PDB:6UEL"
FT STRAND 1027..1032
FT /evidence="ECO:0007829|PDB:6UEL"
FT HELIX 1037..1047
FT /evidence="ECO:0007829|PDB:6UEL"
FT STRAND 1050..1053
FT /evidence="ECO:0007829|PDB:6UEL"
FT STRAND 1055..1057
FT /evidence="ECO:0007829|PDB:6UEL"
FT HELIX 1059..1063
FT /evidence="ECO:0007829|PDB:6UEL"
FT HELIX 1065..1070
FT /evidence="ECO:0007829|PDB:6UEL"
FT HELIX 1080..1087
FT /evidence="ECO:0007829|PDB:6UEL"
FT HELIX 1089..1098
FT /evidence="ECO:0007829|PDB:6UEL"
FT STRAND 1106..1111
FT /evidence="ECO:0007829|PDB:6UEL"
FT HELIX 1112..1121
FT /evidence="ECO:0007829|PDB:6UEL"
FT STRAND 1126..1129
FT /evidence="ECO:0007829|PDB:5DOT"
FT STRAND 1140..1142
FT /evidence="ECO:0007829|PDB:5DOT"
FT HELIX 1145..1151
FT /evidence="ECO:0007829|PDB:5DOT"
FT STRAND 1164..1168
FT /evidence="ECO:0007829|PDB:6UEL"
FT STRAND 1174..1183
FT /evidence="ECO:0007829|PDB:6UEL"
FT STRAND 1186..1197
FT /evidence="ECO:0007829|PDB:6UEL"
FT STRAND 1199..1201
FT /evidence="ECO:0007829|PDB:6W2J"
FT STRAND 1203..1205
FT /evidence="ECO:0007829|PDB:6UEL"
FT STRAND 1208..1211
FT /evidence="ECO:0007829|PDB:6UEL"
FT HELIX 1217..1233
FT /evidence="ECO:0007829|PDB:6UEL"
FT STRAND 1238..1247
FT /evidence="ECO:0007829|PDB:6UEL"
FT STRAND 1250..1259
FT /evidence="ECO:0007829|PDB:6UEL"
FT HELIX 1264..1271
FT /evidence="ECO:0007829|PDB:6UEL"
FT HELIX 1275..1284
FT /evidence="ECO:0007829|PDB:6UEL"
FT STRAND 1296..1298
FT /evidence="ECO:0007829|PDB:6UEL"
FT STRAND 1306..1310
FT /evidence="ECO:0007829|PDB:6UEL"
FT STRAND 1312..1319
FT /evidence="ECO:0007829|PDB:6UEL"
FT STRAND 1321..1324
FT /evidence="ECO:0007829|PDB:6UEL"
FT STRAND 1326..1332
FT /evidence="ECO:0007829|PDB:6UEL"
FT STRAND 1335..1341
FT /evidence="ECO:0007829|PDB:6UEL"
FT HELIX 1342..1352
FT /evidence="ECO:0007829|PDB:6UEL"
FT STRAND 1360..1365
FT /evidence="ECO:0007829|PDB:6UEL"
FT HELIX 1368..1370
FT /evidence="ECO:0007829|PDB:6UEL"
FT HELIX 1371..1383
FT /evidence="ECO:0007829|PDB:6UEL"
FT STRAND 1387..1391
FT /evidence="ECO:0007829|PDB:6UEL"
FT HELIX 1392..1400
FT /evidence="ECO:0007829|PDB:6UEL"
FT STRAND 1406..1408
FT /evidence="ECO:0007829|PDB:6UEL"
FT HELIX 1411..1413
FT /evidence="ECO:0007829|PDB:6UEL"
FT STRAND 1418..1421
FT /evidence="ECO:0007829|PDB:5DOT"
FT HELIX 1423..1428
FT /evidence="ECO:0007829|PDB:6UEL"
FT STRAND 1434..1437
FT /evidence="ECO:0007829|PDB:6UEL"
FT HELIX 1443..1445
FT /evidence="ECO:0007829|PDB:2YVQ"
FT HELIX 1446..1459
FT /evidence="ECO:0007829|PDB:6UEL"
FT HELIX 1467..1479
FT /evidence="ECO:0007829|PDB:6UEL"
FT TURN 1486..1491
FT /evidence="ECO:0007829|PDB:5DOT"
FT CONFLICT P31327-3:5
FT /note="I -> IF (in Ref. 11; BAD92037)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1500 AA; 164939 MW; E53A22D77563961D CRC64;
MTRILTAFKV VRTLKTGFGF TNVTAHQKWK FSRPGIRLLS VKAQTAHIVL EDGTKMKGYS
FGHPSSVAGE VVFNTGLGGY PEAITDPAYK GQILTMANPI IGNGGAPDTT ALDELGLSKY
LESNGIKVSG LLVLDYSKDY NHWLATKSLG QWLQEEKVPA IYGVDTRMLT KIIRDKGTML
GKIEFEGQPV DFVDPNKQNL IAEVSTKDVK VYGKGNPTKV VAVDCGIKNN VIRLLVKRGA
EVHLVPWNHD FTKMEYDGIL IAGGPGNPAL AEPLIQNVRK ILESDRKEPL FGISTGNLIT
GLAAGAKTYK MSMANRGQNQ PVLNITNKQA FITAQNHGYA LDNTLPAGWK PLFVNVNDQT
NEGIMHESKP FFAVQFHPEV TPGPIDTEYL FDSFFSLIKK GKATTITSVL PKPALVASRV
EVSKVLILGS GGLSIGQAGE FDYSGSQAVK AMKEENVKTV LMNPNIASVQ TNEVGLKQAD
TVYFLPITPQ FVTEVIKAEQ PDGLILGMGG QTALNCGVEL FKRGVLKEYG VKVLGTSVES
IMATEDRQLF SDKLNEINEK IAPSFAVESI EDALKAADTI GYPVMIRSAY ALGGLGSGIC
PNRETLMDLS TKAFAMTNQI LVEKSVTGWK EIEYEVVRDA DDNCVTVCNM ENVDAMGVHT
GDSVVVAPAQ TLSNAEFQML RRTSINVVRH LGIVGECNIQ FALHPTSMEY CIIEVNARLS
RSSALASKAT GYPLAFIAAK IALGIPLPEI KNVVSGKTSA CFEPSLDYMV TKIPRWDLDR
FHGTSSRIGS SMKSVGEVMA IGRTFEESFQ KALRMCHPSI EGFTPRLPMN KEWPSNLDLR
KELSEPSSTR IYAIAKAIDD NMSLDEIEKL TYIDKWFLYK MRDILNMEKT LKGLNSESMT
EETLKRAKEI GFSDKQISKC LGLTEAQTRE LRLKKNIHPW VKQIDTLAAE YPSVTNYLYV
TYNGQEHDVN FDDHGMMVLG CGPYHIGSSV EFDWCAVSSI RTLRQLGKKT VVVNCNPETV
STDFDECDKL YFEELSLERI LDIYHQEACG GCIISVGGQI PNNLAVPLYK NGVKIMGTSP
LQIDRAEDRS IFSAVLDELK VAQAPWKAVN TLNEALEFAK SVDYPCLLRP SYVLSGSAMN
VVFSEDEMKK FLEEATRVSQ EHPVVLTKFV EGAREVEMDA VGKDGRVISH AISEHVEDAG
VHSGDATLML PTQTISQGAI EKVKDATRKI AKAFAISGPF NVQFLVKGND VLVIECNLRA
SRSFPFVSKT LGVDFIDVAT KVMIGENVDE KHLPTLDHPI IPADYVAIKA PMFSWPRLRD
ADPILRCEMA STGEVACFGE GIHTAFLKAM LSTGFKIPQK GILIGIQQSF RPRFLGVAEQ
LHNEGFKLFA TEATSDWLNA NNVPATPVAW PSQEGQNPSL SSIRKLIRDG SIDLVINLPN
NNTKFVHDNY VIRRTAVDSG IPLLTNFQVT KLFAEAVQKS RKVDSKSLFH YRQYSAGKAA
